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dc.contributor.authorKerselidou, Despoina
dc.contributor.authorDohai, Bushra Saeed
dc.contributor.authorNelson, David R.
dc.contributor.authorDaakour, Sarah
dc.contributor.authorDe Cock, Nicolas
dc.contributor.authorHassoun, Zahra Al Oula
dc.contributor.authorKim, Dae-Kyum
dc.contributor.authorOlivet, Julien
dc.contributor.authorEl Assal, Diana C.
dc.contributor.authorJaiswal, Ashish
dc.contributor.authorAlzahmi, Amnah
dc.contributor.authorSaha, Deeya
dc.contributor.authorPain, Charlotte
dc.contributor.authorMatthijssens, Filip
dc.contributor.authorLemaitre, Pierre
dc.contributor.authorHerfs, Michael
dc.contributor.authorChapuis, Julien
dc.contributor.authorGhesquiere, Bart
dc.contributor.authorVertommen, Didier
dc.contributor.authorKriechbaumer, Verena
dc.contributor.authorKnoops, Kèvin
dc.contributor.authorLopez-Iglesias, Carmen
dc.contributor.authorvan Zandvoort, Marc
dc.contributor.authorLambert, Jean-Charles
dc.contributor.authorHanson, Julien
dc.contributor.authorDesmet, Christophe
dc.contributor.authorThiry, Marc
dc.contributor.authorLauersen, Kyle J.
dc.contributor.authorVidal, Marc
dc.contributor.authorVan Vlierberghe, Pieter
dc.contributor.authorDequiedt, Franck
dc.contributor.authorSalehi-Ashtiani, Kourosh
dc.contributor.authorTwizere, Jean-Claude
dc.date.accessioned2021-05-11T09:21:15Z
dc.date.available2021-05-11T09:21:15Z
dc.date.issued2021-05-07
dc.date.submitted2020-09-27
dc.identifier.citationKerselidou, D., Dohai, B. S., Nelson, D. R., Daakour, S., De Cock, N., Hassoun, Z. A. O., … Twizere, J.-C. (2021). Alternative glycosylation controls endoplasmic reticulum dynamics and tubular extension in mammalian cells. Science Advances, 7(19), eabe8349. doi:10.1126/sciadv.abe8349
dc.identifier.issn2375-2548
dc.identifier.pmid33962942
dc.identifier.doi10.1126/sciadv.abe8349
dc.identifier.urihttp://hdl.handle.net/10754/669164
dc.description.abstractThe endoplasmic reticulum (ER) is a central eukaryotic organelle with a tubular network made of hairpin proteins linked by hydrolysis of guanosine triphosphate nucleotides. Among posttranslational modifications initiated at the ER level, glycosylation is the most common reaction. However, our understanding of the impact of glycosylation on the ER structure remains unclear. Here, we show that exostosin-1 (EXT1) glycosyltransferase, an enzyme involved in N-glycosylation, is a key regulator of ER morphology and dynamics. We have integrated multiomics and superresolution imaging to characterize the broad effect of EXT1 inactivation, including the ER shape-dynamics-function relationships in mammalian cells. We have observed that inactivating EXT1 induces cell enlargement and enhances metabolic switches such as protein secretion. In particular, suppressing EXT1 in mouse thymocytes causes developmental dysfunctions associated with the ER network extension. Last, our data illuminate the physical and functional aspects of the ER proteome-glycome-lipidome structure axis, with implications in biotechnology and medicine.
dc.description.sponsorshipD.-K.K. was supported by Banting Postdoctoral Fellowship of Canada and Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2017R1A6A3A03004385). B.S.D., S.D., D.R.N., A.J., D.C.E.A., and K.S.-A. were supported by New York University Abu Dhabi (NYUAD) Institute grant 73 71210 CGSB9 and NYUAD Faculty Research Fund AD060. D.K. was supported by an FRS-FNRS-Télévie Fellowship no. 7651317F (J.-C.T.). J.-C.T. is a Maitre de Recherche of the FRS-FNRS. Primarily, the Fonds de la Recherche Scientifique (FRS-FNRS) and the Fonds Leon Fredericq grants supported this work.
dc.publisherAmerican Association for the Advancement of Science (AAAS)
dc.relation.urlhttps://advances.sciencemag.org/lookup/doi/10.1126/sciadv.abe8349
dc.rightsExclusive licensee American Association for the Advancement of Science. No claim to original U.S.Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.titleAlternative glycosylation controls endoplasmic reticulum dynamics and tubular extension in mammalian cells
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering Division (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Kingdom of Saudi Arabia.
dc.identifier.journalScience Advances
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionLaboratory of Viral Interactomes, GIGA Institute, University of Liege, Liege, Belgium.
dc.contributor.institutionLaboratory of Gene expression and Cancer, GIGA Institute, University of Liege, Liege, Belgium.
dc.contributor.institutionDivision of Science and Math, New York University Abu Dhabi, Abu Dhabi, UAE.
dc.contributor.institutionCenter for Genomics and Systems Biology (CGSB), New York University Abu Dhabi, Abu Dhabi, UAE.
dc.contributor.institutionTERRA Teaching and Research Centre, University of Liege, Liege, Belgium.
dc.contributor.institutionThe Donnelly Centre, University of Toronto, Toronto, ON, Canada.
dc.contributor.institutionDepartment of Molecular Genetics, University of Toronto, Toronto, ON, Canada.
dc.contributor.institutionLunenfeld Tanenbaum Research Institute, Mount Sinai Hospital, Toronto, ON, Canada.
dc.contributor.institutionPlant Cell Biology, Biological and Medical Sciences, Oxford Brookes University, Oxford, UK.
dc.contributor.institutionDepartment of Biomolecular Medicine and Center for Medical Genetics, Ghent University, Ghent, Belgium.
dc.contributor.institutionCancer Research Institute Ghent (CRIG), Ghent, Belgium.
dc.contributor.institutionGIGA-I3 Unit, GIGA Institute, University of Liege, Liege, Belgium.
dc.contributor.institutionGIGA-Cancer Unit, GIGA Institute, University of Liege, Liege, Belgium.
dc.contributor.institutionLaboratory of Excellence Distalz, INSERM Unit 1167, Pasteur Institute of Lille, Lille, France.
dc.contributor.institutionMetabolomics Expertise Center, Center for Cancer Biology, VIB Center for Cancer Biology, Leuven, Belgium.
dc.contributor.institutionde Duve Institute, Catholic University of Louvain, Brussels, Belgium.
dc.contributor.institutionMicroscopy CORE Lab, Maastricht Multimodal Molecular Imaging Institute, Maastricht University, Maastricht, Netherlands.
dc.contributor.institutionDepartment of Cell Biology, School for Cardiovascular Diseases (CARIM), School for Nutrition and Translational Research in Metabolism (NUTRIM), School for Mental health and Neuroscience (MHeNS), and School for Oncology and Developmental Biology (GROW), Maastricht University, Maastricht, Netherlands.
dc.contributor.institutionGIGA-Molecular Pharmacology, University of Liege, Liege, Belgium.
dc.contributor.institutionLaboratory of cell and tissue Biology, GIGA-Neurosciences, University of Liege, Liege, Belgium.
dc.contributor.institutionCenter for Cancer Systems Biology (CCSB), Dana-Farber Cancer Institute, Boston, MA, USA.
dc.contributor.institutionDepartment of Genetics, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.
dc.identifier.volume7
dc.identifier.issue19
dc.identifier.pageseabe8349
kaust.personLauersen, Kyle J.
dc.date.accepted2021-03-18
refterms.dateFOA2021-05-11T09:29:02Z


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Exclusive licensee American Association for the Advancement of Science. No claim to original U.S.Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).
Except where otherwise noted, this item's license is described as Exclusive licensee American Association for the Advancement of Science. No claim to original U.S.Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).